1QI4

MUTANT (E219G) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX WITH MALTOTETRAOSE

Summary for 1QI4

Related PRD IDPRD_900010
DescriptorPROTEIN (EXO-MALTOTETRAOHYDROLASE), alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
Functional Keywordshydrolase, maltotetraose-forming exo amylase
Biological sourcePseudomonas stutzeri
Cellular locationSecreted  P13507
Total number of polymer chains1
Total molecular weight48084.29
Authors
Hasegawa, K.,Kubota, M.,Matsuura, Y. (deposition date: 1999-06-01, release date: 1999-11-24, Last modification date: 2020-07-29)
Primary citation
Hasegawa, K.,Kubota, M.,Matsuura, Y.
Roles of catalytic residues in alpha-amylases as evidenced by the structures of the product-complexed mutants of a maltotetraose-forming amylase.
Protein Eng., 12:819-824, 1999
PubMed: 10556241 (PDB entries with the same primary citation)
DOI: 10.1093/protein/12.10.819
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers14 0.2% 6.9% 1.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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171588
PDB entries from 2020-11-25